TM10C_HUMAN
ID TM10C_HUMAN Reviewed; 403 AA.
AC Q7L0Y3; Q9NRG5; Q9NX54; Q9Y596;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=tRNA methyltransferase 10 homolog C {ECO:0000305};
DE AltName: Full=HBV pre-S2 trans-regulated protein 2 {ECO:0000303|PubMed:12546731};
DE AltName: Full=Mitochondrial ribonuclease P protein 1 {ECO:0000303|PubMed:18984158};
DE Short=Mitochondrial RNase P protein 1 {ECO:0000303|PubMed:18984158};
DE AltName: Full=RNA (guanine-9-)-methyltransferase domain-containing protein 1;
DE AltName: Full=Renal carcinoma antigen NY-REN-49 {ECO:0000303|PubMed:10508479};
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase {ECO:0000303|PubMed:29072297};
DE EC=2.1.1.- {ECO:0000269|PubMed:29072297};
DE AltName: Full=tRNA (adenine(9)-N(1))-methyltransferase;
DE EC=2.1.1.218 {ECO:0000269|PubMed:23042678};
DE AltName: Full=tRNA (guanine(9)-N(1))-methyltransferase;
DE EC=2.1.1.221 {ECO:0000269|PubMed:23042678};
DE Flags: Precursor;
GN Name=TRMT10C {ECO:0000312|HGNC:HGNC:26022};
GN Synonyms=MRPP1 {ECO:0000303|PubMed:18984158}, RG9MTD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human liver cancer tissue.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Signet-ring cell carcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-129, IDENTIFICATION AS A RENAL CANCER
RP ANTIGEN, AND VARIANT ARG-56.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-403.
RX PubMed=12546731;
RA Lu Y.Y., Li K., Wang L., Liu Y., Wang Y.D., Cheng J., Zhang L.X.;
RT "Screening of the genes of hepatitis B virus preS2 interacting proteins.";
RL Zhonghua Gan Zang Bing Za Zhi 11:8-10(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH HSD17B10
RP AND KIAA0391, AND SUBCELLULAR LOCATION.
RX PubMed=18984158; DOI=10.1016/j.cell.2008.09.013;
RA Holzmann J., Frank P., Loeffler E., Bennett K.L., Gerner C., Rossmanith W.;
RT "RNase P without RNA: identification and functional reconstitution of the
RT human mitochondrial tRNA processing enzyme.";
RL Cell 135:462-474(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION.
RX PubMed=21593607; DOI=10.4161/rna.8.4.15393;
RA Brzezniak L.K., Bijata M., Szczesny R.J., Stepien P.P.;
RT "Involvement of human ELAC2 gene product in 3' end processing of
RT mitochondrial tRNAs.";
RL RNA Biol. 8:616-626(2011).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HSD17B10, AND MUTAGENESIS OF
RP ASP-314.
RX PubMed=23042678; DOI=10.1093/nar/gks910;
RA Vilardo E., Nachbagauer C., Buzet A., Taschner A., Holzmann J.,
RA Rossmanith W.;
RT "A subcomplex of human mitochondrial RNase P is a bifunctional
RT methyltransferase--extensive moonlighting in mitochondrial tRNA
RT biogenesis.";
RL Nucleic Acids Res. 40:11583-11593(2012).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GRSF1.
RX PubMed=23473034; DOI=10.1016/j.cmet.2013.02.005;
RA Jourdain A.A., Koppen M., Wydro M., Rodley C.D., Lightowlers R.N.,
RA Chrzanowska-Lightowlers Z.M., Martinou J.C.;
RT "GRSF1 regulates RNA processing in mitochondrial RNA granules.";
RL Cell Metab. 17:399-410(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24703694; DOI=10.1016/j.cmet.2014.03.013;
RA Bogenhagen D.F., Martin D.W., Koller A.;
RT "Initial steps in RNA processing and ribosome assembly occur at
RT mitochondrial DNA nucleoids.";
RL Cell Metab. 19:618-629(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP FUNCTION, INVOLVEMENT IN COXPD30, VARIANTS COXPD30 LEU-181 AND ALA-272, AND
RP CHARACTERIZATION OF VARIANTS COXPD30 LEU-181 AND ALA-272.
RX PubMed=27132592; DOI=10.1016/j.ajhg.2016.03.010;
RA Metodiev M.D., Thompson K., Alston C.L., Morris A.A., He L., Assouline Z.,
RA Rio M., Bahi-Buisson N., Pyle A., Griffin H., Siira S., Filipovska A.,
RA Munnich A., Chinnery P.F., McFarland R., Roetig A., Taylor R.W.;
RT "Recessive mutations in TRMT10C cause defects in mitochondrial RNA
RT processing and multiple respiratory chain deficiencies.";
RL Am. J. Hum. Genet. 98:993-1000(2016).
RN [16]
RP CAUTION.
RX PubMed=29107537; DOI=10.1016/j.molcel.2017.10.019;
RA Li X., Xiong X., Zhang M., Wang K., Chen Y., Zhou J., Mao Y., Lv J., Yi D.,
RA Chen X.W., Wang C., Qian S.B., Yi C.;
RT "Base-resolution mapping reveals distinct m1A methylome in nuclear- and
RT mitochondrial-encoded transcripts.";
RL Mol. Cell 0:0-0(2017).
RN [17]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29072297; DOI=10.1038/nature24456;
RA Safra M., Sas-Chen A., Nir R., Winkler R., Nachshon A., Bar-Yaacov D.,
RA Erlacher M., Rossmanith W., Stern-Ginossar N., Schwartz S.;
RT "The m(1)A landscape on cytosolic and mitochondrial mRNA at single-base
RT resolution.";
RL Nature 551:251-255(2017).
RN [18]
RP FUNCTION, AND INTERACTION WITH HSD17B10.
RX PubMed=29040705; DOI=10.1093/nar/gkx902;
RA Reinhard L., Sridhara S., Haellberg B.M.;
RT "The MRPP1/MRPP2 complex is a tRNA-maturation platform in human
RT mitochondria.";
RL Nucleic Acids Res. 45:12469-12480(2017).
CC -!- FUNCTION: Mitochondrial tRNA N(1)-methyltransferase involved in
CC mitochondrial tRNA maturation (PubMed:18984158, PubMed:21593607,
CC PubMed:23042678, PubMed:27132592). Component of mitochondrial
CC ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and
CC PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends
CC (PubMed:18984158). Together with HSD17B10/MRPP2, forms a subcomplex of
CC the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which
CC displays functions that are independent of the ribonuclease P activity
CC (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex
CC catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at
CC position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting
CC as the catalytic N(1)-methyltransferase subunit (PubMed:23042678). The
CC MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform:
CC following 5'-end cleavage by the mitochondrial ribonuclease P complex,
CC the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing
CC catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and
CC presents the nascent tRNA to the mitochondrial CCA tRNA
CC nucleotidyltransferase TRNT1 enzyme (PubMed:29040705). In addition to
CC tRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA
CC N(1)-methyltransferase by mediating methylation of adenosine residues
CC at the N(1) position of MT-ND5 mRNA (PubMed:29072297). Associates with
CC mitochondrial DNA complexes at the nucleoids to initiate RNA processing
CC and ribosome assembly. {ECO:0000269|PubMed:18984158,
CC ECO:0000269|PubMed:21593607, ECO:0000269|PubMed:23042678,
CC ECO:0000269|PubMed:24703694, ECO:0000269|PubMed:27132592,
CC ECO:0000269|PubMed:29040705, ECO:0000269|PubMed:29072297}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43148, Rhea:RHEA-COMP:10363, Rhea:RHEA-COMP:10364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.218;
CC Evidence={ECO:0000269|PubMed:23042678};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC Evidence={ECO:0000269|PubMed:23042678};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(1)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55392, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12415,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491;
CC Evidence={ECO:0000269|PubMed:29072297};
CC -!- SUBUNIT: Component of mitochondrial ribonuclease P, a complex composed
CC of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3.(PubMed:18984158).
CC Interacts with HSD17B10/MRPP2; forming the MRPP1-MRPP2 subcomplex of
CC the mitochondrial ribonuclease P complex (PubMed:23042678,
CC PubMed:29040705). Interacts with GRSF1 (PubMed:23473034).
CC {ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:23042678,
CC ECO:0000269|PubMed:23473034, ECO:0000269|PubMed:29040705}.
CC -!- INTERACTION:
CC Q7L0Y3; Q99714: HSD17B10; NbExp=22; IntAct=EBI-2107046, EBI-79964;
CC Q7L0Y3; Q7L0Y3: TRMT10C; NbExp=2; IntAct=EBI-2107046, EBI-2107046;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:23473034,
CC ECO:0000269|PubMed:24703694}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 30 (COXPD30)
CC [MIM:616974]: An autosomal recessive, severe mitochondrial disease
CC characterized by lactic acidosis, hypotonia, feeding difficulties,
CC deafness, and respiratory failure with fatal issue. Patient skeletal
CC muscle cells show decreased activities of mitochondrial complexes I,
CC III and IV. {ECO:0000269|PubMed:27132592}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
CC -!- CAUTION: The identity of the enzyme catalyzing mitochondrial mRNA N(1)-
CC methyltransferase is unclear. According to a report, mitochondrial mRNA
CC N(1)-methyltransferase activity is catalyzed by TRMT61B (AC Q9BVS5)
CC (PubMed:29107537). According to a second report, it is mediated by
CC TRMT10C (PubMed:29072297). As both reports only tested one protein
CC (either TRMT61B or TRMT10C), it is possible that both proteins have
CC this activity. {ECO:0000269|PubMed:29072297,
CC ECO:0000269|PubMed:29107537}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD42877.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH35967.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91166.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF226052; AAF86952.1; -; mRNA.
DR EMBL; AK000439; BAA91166.1; ALT_FRAME; mRNA.
DR EMBL; CH471052; EAW79795.1; -; Genomic_DNA.
DR EMBL; BC035967; AAH35967.2; ALT_INIT; mRNA.
DR EMBL; AF155111; AAD42877.1; ALT_INIT; mRNA.
DR EMBL; AY561707; AAS66980.1; -; mRNA.
DR CCDS; CCDS43122.1; -.
DR RefSeq; NP_060289.2; NM_017819.3.
DR PDB; 5NFJ; X-ray; 1.96 A; A/B/C=203-403.
DR PDB; 7ONU; EM; 3.00 A; F=40-403.
DR PDBsum; 5NFJ; -.
DR PDBsum; 7ONU; -.
DR AlphaFoldDB; Q7L0Y3; -.
DR SMR; Q7L0Y3; -.
DR BioGRID; 120271; 179.
DR ComplexPortal; CPX-6155; Mitochondrial ribonuclease P complex.
DR ComplexPortal; CPX-6161; Mitochondrial tRNA:m(1)R9 methyltransferase complex.
DR CORUM; Q7L0Y3; -.
DR IntAct; Q7L0Y3; 57.
DR MINT; Q7L0Y3; -.
DR STRING; 9606.ENSP00000312356; -.
DR MoonProt; Q7L0Y3; -.
DR GlyGen; Q7L0Y3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7L0Y3; -.
DR MetOSite; Q7L0Y3; -.
DR PhosphoSitePlus; Q7L0Y3; -.
DR SwissPalm; Q7L0Y3; -.
DR BioMuta; TRMT10C; -.
DR DMDM; 221222465; -.
DR EPD; Q7L0Y3; -.
DR jPOST; Q7L0Y3; -.
DR MassIVE; Q7L0Y3; -.
DR MaxQB; Q7L0Y3; -.
DR PaxDb; Q7L0Y3; -.
DR PeptideAtlas; Q7L0Y3; -.
DR PRIDE; Q7L0Y3; -.
DR ProteomicsDB; 68741; -.
DR TopDownProteomics; Q7L0Y3; -.
DR Antibodypedia; 32284; 83 antibodies from 18 providers.
DR DNASU; 54931; -.
DR Ensembl; ENST00000309922.7; ENSP00000312356.6; ENSG00000174173.7.
DR GeneID; 54931; -.
DR KEGG; hsa:54931; -.
DR MANE-Select; ENST00000309922.7; ENSP00000312356.6; NM_017819.4; NP_060289.2.
DR UCSC; uc003duz.5; human.
DR CTD; 54931; -.
DR DisGeNET; 54931; -.
DR GeneCards; TRMT10C; -.
DR HGNC; HGNC:26022; TRMT10C.
DR HPA; ENSG00000174173; Low tissue specificity.
DR MalaCards; TRMT10C; -.
DR MIM; 615423; gene.
DR MIM; 616974; phenotype.
DR neXtProt; NX_Q7L0Y3; -.
DR OpenTargets; ENSG00000174173; -.
DR Orphanet; 478042; Combined oxidative phosphorylation defect type 30.
DR PharmGKB; PA134988378; -.
DR VEuPathDB; HostDB:ENSG00000174173; -.
DR eggNOG; KOG2967; Eukaryota.
DR GeneTree; ENSGT00530000063169; -.
DR HOGENOM; CLU_034384_3_1_1; -.
DR InParanoid; Q7L0Y3; -.
DR OMA; IDPFHIY; -.
DR OrthoDB; 1569668at2759; -.
DR PhylomeDB; Q7L0Y3; -.
DR TreeFam; TF319795; -.
DR BRENDA; 2.1.1.218; 2681.
DR BRENDA; 2.1.1.221; 2681.
DR PathwayCommons; Q7L0Y3; -.
DR Reactome; R-HSA-6785470; tRNA processing in the mitochondrion.
DR Reactome; R-HSA-6787450; tRNA modification in the mitochondrion.
DR Reactome; R-HSA-8868766; rRNA processing in the mitochondrion.
DR SignaLink; Q7L0Y3; -.
DR BioGRID-ORCS; 54931; 249 hits in 1088 CRISPR screens.
DR ChiTaRS; TRMT10C; human.
DR GenomeRNAi; 54931; -.
DR Pharos; Q7L0Y3; Tbio.
DR PRO; PR:Q7L0Y3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q7L0Y3; protein.
DR Bgee; ENSG00000174173; Expressed in left ventricle myocardium and 190 other tissues.
DR ExpressionAtlas; Q7L0Y3; baseline and differential.
DR Genevisible; Q7L0Y3; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:CAFA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0061953; F:mRNA (adenine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IDA:CAFA.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IDA:CAFA.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0000964; P:mitochondrial RNA 5'-end processing; IMP:UniProtKB.
DR GO; GO:1990180; P:mitochondrial tRNA 3'-end processing; IDA:UniProtKB.
DR GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; IDA:UniProtKB.
DR GO; GO:0070901; P:mitochondrial tRNA methylation; IDA:ComplexPortal.
DR GO; GO:0090646; P:mitochondrial tRNA processing; IMP:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:UniProtKB.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR025812; TRM10C.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR PANTHER; PTHR13563:SF5; PTHR13563:SF5; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Disease variant; Methyltransferase;
KW Mitochondrion; Mitochondrion nucleoid; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..403
FT /note="tRNA methyltransferase 10 homolog C"
FT /id="PRO_0000311309"
FT DOMAIN 191..383
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT COILED 138..169
FT /evidence="ECO:0000255"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UFY8"
FT VARIANT 56
FT /note="P -> R (in dbSNP:rs3762735)"
FT /evidence="ECO:0000269|PubMed:10508479"
FT /id="VAR_057355"
FT VARIANT 164
FT /note="K -> N (in dbSNP:rs16844031)"
FT /id="VAR_057356"
FT VARIANT 181
FT /note="R -> L (in COXPD30; decreased protein abundance;
FT impaired mitochondrial tRNA processing; has no effect on
FT steady-state mitochondrial-mRNA and mitochondrial-tRNA
FT levels but indirectly impairs mitochondrial translation;
FT dbSNP:rs199730889)"
FT /evidence="ECO:0000269|PubMed:27132592"
FT /id="VAR_076993"
FT VARIANT 272
FT /note="T -> A (in COXPD30; decreased protein abundance;
FT impaired mitochondrial tRNA processing; has no effect on
FT steady-state mitochondrial-mRNA and mitochondrial-tRNA
FT levels but indirectly impairs mitochondrial translation;
FT dbSNP:rs875989831)"
FT /evidence="ECO:0000269|PubMed:27132592"
FT /id="VAR_076994"
FT MUTAGEN 314
FT /note="D->N: Abolished mitochondrial tRNA methylation. Does
FT not affect mitochondrial tRNA 5'-end processing."
FT /evidence="ECO:0000269|PubMed:23042678"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 126..155
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 183..201
FT /evidence="ECO:0007829|PDB:7ONU"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 217..236
FT /evidence="ECO:0007829|PDB:5NFJ"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:7ONU"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:5NFJ"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:5NFJ"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:5NFJ"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:5NFJ"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:5NFJ"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7ONU"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:5NFJ"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:5NFJ"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:5NFJ"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 353..364
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:5NFJ"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:5NFJ"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:7ONU"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:7ONU"
SQ SEQUENCE 403 AA; 47347 MW; 28CBD97B4114819F CRC64;
MAAFLKMSVS VNFFRPFTRF LVPFTLHRKR NNLTILQRYM SSKIPAVTYP KNESTPPSEE
LELDKWKTTM KSSVQEECVS TISSSKDEDP LAATREFIEM WRLLGREVPE HITEEELKTL
MECVSNTAKK KYLKYLYTKE KVKKARQIKK EMKAAAREEA KNIKLLETTE EDKQKNFLFL
RLWDRNMDIA MGWKGAQAMQ FGQPLVFDMA YENYMKRKEL QNTVSQLLES EGWNRRNVDP
FHIYFCNLKI DGALHRELVK RYQEKWDKLL LTSTEKSHVD LFPKDSIIYL TADSPNVMTT
FRHDKVYVIG SFVDKSMQPG TSLAKAKRLN LATECLPLDK YLQWEIGNKN LTLDQMIRIL
LCLKNNGNWQ EALQFVPKRK HTGFLEISQH SQEFINRLKK AKT
